1998
Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II
Shao W, Fernandez E, Wilken J, Thompson D, Siani M, West J, Lolis E, Schweitzer B. Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II. FEBS Letters 1998, 441: 77-82. PMID: 9877169, DOI: 10.1016/s0014-5793(98)01520-8.Peer-Reviewed Original ResearchConceptsTotal chemical synthesisNuclear magnetic resonanceChemical synthesisX-ray crystallographyThree-dimensional structureStructural studiesSynthesisSecondary structureGenome programNew proteinsMagnetic resonanceSelenomethionine proteinsRecombinant proteinsProtein IIHeavy-atom derivativesProteinMIP IICrystallographyMonomersStructureDeterminationDerivativesCloningHigh resolutionResonanceDirect link between cytokine activity and a catalytic site for macrophage migration inhibitory factor
Swope M, Sun H, Blake P, Lolis E. Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor. The EMBO Journal 1998, 17: 3534-3541. PMID: 9649424, PMCID: PMC1170690, DOI: 10.1093/emboj/17.13.3534.Peer-Reviewed Original ResearchConceptsN-terminal prolineN-terminal regionStructure-based inhibitorsMultiple sequence alignmentThree-dimensional structureInvariant residuesEntire polypeptideMicrobial enzymesCatalytic basePro-1Sequence alignmentMIF homologuesCytokine activityHuman macrophage migration inhibitory factorCatalytic siteProlineInhibitory factorHomologuesUnderlying biological activityP-hydroxyphenylpyruvateProteinMacrophage migration inhibitory factorActive siteBiological activity
1996
Structure-Function Studies of Murine MIP-2, the Homologue of Melanoma Growth Stimulating Activity/gro-α and IL-8
Lolis E, Jerva L. Structure-Function Studies of Murine MIP-2, the Homologue of Melanoma Growth Stimulating Activity/gro-α and IL-8. NATO ASI Series 1996, 183-194. DOI: 10.1007/978-3-642-61180-3_17.Peer-Reviewed Original ResearchHuman melanoma cellsProtein 2Structure-function studiesAnalysis of sequencesLigand-receptor complexesMurine MIP-2Melanoma cellsThree-dimensional structureMurine homologueGene productsAmino terminusMutational analysisInflammatory protein-2Molecular mechanismsIL-8MIP-2High affinityProteinAutocrine growth factorBinding profileHomologuesMetastatic potentialGrowth factorMelanoma growthType B receptors
1994
Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site.
Joseph-McCarthy D, Lolis E, Komives E, Petsko G. Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site. Biochemistry 1994, 33: 2815-23. PMID: 8130194, DOI: 10.1021/bi00176a010.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesCrystallizationCrystallography, X-RayDNA PrimersLigandsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPoint MutationProtein FoldingProtein Structure, SecondaryRecombinant ProteinsSaccharomyces cerevisiaeTriose-Phosphate IsomeraseX-Ray DiffractionConceptsMutant enzymesSubstrate-binding loopActive-site LysLys-12Wild-type enzymeMet side chainsActive siteEnzyme-inhibitor complexThree-dimensional structureMutant structuresWild typeTriosephosphate isomeraseDianionic substrateEnzymeSame crystal formCrystal structureMET mutationsSide chainsIsomeraseSitesCrystal formsMutationsPhosphoglycolohydroxamateMethionine